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Activation of phospholipase C‐Ca 2+ system by sphingosine 1‐phosphate in CHO cells transfected with Edg‐3, a putative lipid receptor
Author(s) -
Sato Koichi,
Kon Junko,
Tomura Hideaki,
Osada Mizuho,
Murata Naoya,
Kuwabara Atsushi,
Watanabe Tomoko,
Ohta Hideo,
Ui Michio,
Okajima Fumikazu
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01676-7
Subject(s) - transfection , phospholipase c , sphingosine , inositol phosphate , sphingosine 1 phosphate , inositol , receptor , chinese hamster ovary cell , sphingosine 1 phosphate receptor , phospholipase , biochemistry , chemistry , biology , microbiology and biotechnology , enzyme , gene
Sphingosine 1‐phosphate (S1P) induces phospholipase C (PLC) activation and Ca 2+ mobilization in many types of cells. We examined the possible involvement of Edg‐3, one of the putative S1P receptors, in the phospholipase C (PLC)‐Ca 2+ system. S1P increased the cytoplasmic free Ca 2+ concentration without detectable inositol phosphate production in vector‐transfected CHO cells. In the Edg‐3‐transfected cells, however, the S1P‐induced Ca 2+ response was clearly enhanced, which was associated with a significant production of inositol phosphate. These S1P‐induced responses in the Edg‐3‐transfected cells were inhibited by U73122, a potent PLC inhibitor. We conclude that Edg‐3 may be one of the S1P receptors participating in the activation of the PLC‐Ca 2+ system.